Participation of a non-covalent phosphointermediate in ATP hydrolysis by the sarcoplasmic reticulum Ca2(+)-cotransport ATPase
With increasing SDS/protein ratios, covalent phosphorylation by ATP and Pi is abolished before ATP hydrolysis (Pi production) ceases. We have shown that the SDS-dependent profiles of the decline in covalent phosphorylation by either substrate are virtually identical, reflecting a common mechanism of...
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Published in | European journal of biochemistry Vol. 192; no. 3; pp. 627 - 631 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
England
24.09.1990
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Subjects | |
Online Access | Get full text |
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Summary: | With increasing SDS/protein ratios, covalent phosphorylation by ATP and Pi is abolished before ATP hydrolysis (Pi production) ceases. We have shown that the SDS-dependent profiles of the decline in covalent phosphorylation by either substrate are virtually identical, reflecting a common mechanism of detergent interaction, while ATP can be hydrolysed via a non-covalent phosphointermediate. Our studies support that the transfer of both terminal Pi from ATP, as well as Pi to its final binding site, is a multistep reaction involving electrostatic interaction with one or more amino acid side chains, including a Lys residue. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-2956 |